1ce6
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(New page: 200px<br /> <applet load="1ce6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ce6, resolution 2.90Å" /> '''MHC CLASS I H-2DB C...)
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Revision as of 14:14, 12 November 2007
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MHC CLASS I H-2DB COMPLEXED WITH A SENDAI VIRUS NUCLEOPROTEIN PEPTIDE
Contents |
Overview
Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-restricted, glycopeptide-specific cytotoxic T cells (CTL) have been shown to display, nonreciprocal patterns of cross-reactivity. Here, we present the crystal, structures of the H-2Db glycopeptide complexes to 2.85 A resolution or, better. In both cases, the glycan is solvent exposed and available for, direct recognition by the T cell receptor (TCR). We have modeled the, complex formed between the MHC-glycopeptide complexes and their respective, TCRs, showing that a single saccharide residue can be accommodated in the, standard TCR-MHC geometry. The models also reveal a possible molecular, basis for the observed cross-reactivity patterns of the CTL clones, which, appear to be influenced by the length of the CDR3 loop and the nature of, the immunizing ligand.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1CE6 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity., Glithero A, Tormo J, Haurum JS, Arsequell G, Valencia G, Edwards J, Springer S, Townsend A, Pao YL, Wormald M, Dwek RA, Jones EY, Elliott T, Immunity. 1999 Jan;10(1):63-74. PMID:10023771
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